| Product Name | Human Chymotrypsinogen B2 (CTRB2) ELISA Kit |
|---|---|
| Description | Human Chymotrypsinogen B2 (CTRB2) ELISA Kit has high sensitivity and excellent specificity for detection of Human CTRB2. No significant cross-reactivity or interference between Human CTRB2 and analogues was observed. Chymotrypsin is a digestive enzyme that can perform proteolysis. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of amide bond (the S1 position) is a tyrosine, tryptophan, or phenylalanine. These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the P1 position) of the enzyme. The hydrophobic and shape complementarity between the peptide substrate S1 sidechain and the enzyme P1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the S1 position.Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. This Human Chymotrypsinogen B2 (CTRB2) ELISA Kit employs a two-site sandwich ELISA to quantitate CTRB2 in samples. An antibody specific for CTRB2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyCTRB2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for CTRB2 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of CTRB2 bound in the initial step. The color development is stopped and the intensity of the color is measured. |
| Synonyms | CTRB2, Chymotrypsin B2 |
| Method | Sandwich ELISA |
| Detection Range | Please inquire |
| Sensitivity | Please inquire |
| Reactivity | Human |
| Sample Types | Cell culture supernatants, Serum, Plasma, Other biological fluids |
| Gene Id | 440387 |
| Storage | 2-8°C |
| Background | Chymotrypsin is a digestive enzyme that can perform proteolysis. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of amide bond (the S1 position) is a tyrosine, tryptophan, or phenylalanine. These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the P1 position) of the enzyme. The hydrophobic and shape complementarity between the peptide substrate S1 sidechain and the enzyme P1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the S1 position.Chymotrypsin is synthesized in the pancreas by protein biosynthesis as a precursor called chymotrypsinogen that is enzymatically inactive. |
| Supplier | Abbkine |
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